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cpsf2  (Bethyl)


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    Structured Review

    Bethyl cpsf2
    Cpsf2, supplied by Bethyl, used in various techniques. Bioz Stars score: 94/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cpsf100/CPSF100+Antibody/pm41335470-46-14-16
    Average 94 stars, based on 26 article reviews
    cpsf2 - by Bioz Stars, 2026-11
    94/100 stars

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    Related Articles

    Western Blot:

    Article Title: The Role of mRNA 3’ end Processing Factors in Regulating Global RNA Pol II Transcription and its Termination
    Article Snippet: Chromatin immunoprecipitation was performed with antibodies against CPSF100, CPSF73 (Bethyl, A301-581A, A301-091A) and RNAPII (Santa Cruz, N-20, CTD). .. Antibodies used for Western Blotting analyses were: Ints11 (Bethyl, A301-274A), GAPDH (GeneTex, GT239), CPSF100, CPSF73, Pcf11, Symplekin, WDR33, CPSF160, CPSF30, CFIm68, CFIm59, CstF64 (Bethyl, A301-581A, A301-091A, A303-706A, A301-464/5A, A301151/2A, A301-580A, A301-584/5A, A301-356/7/8A, A301-359/60A, A301-092/3A). ..

    Article Title: CFIm25 links Alternative Polyadenylation to Glioblastoma Tumor Suppression
    Article Snippet: .. To detect 3′end processing factors by Western blotting, the following primary antibodies from Bethyl Laboratories were used: CPSF160, CPSF100, CPSF73, CPSF30, hFip, CstF77, CstF64τ, CstF50, CFIm68 and CFIm59. .. Other antibodies used include CFIm25 (PTGlabs), CstF64, CFIImPcf11, and Symplekin (Sigma), CFIImClp1 (Epitomics).

    Immunoprecipitation:

    Article Title: Identification of Novel Roles for RNA Binding Proteins in pre-mRNA Processing
    Article Snippet: .. Endogenous immunoprecipitation was used for Fip1 (Bethyl A301-462A), CPSF100 (Bethyl A301-581A), Symplekin (Bethyl A301-465A), Wdr33 (Bethyl BL4833), and CFIm68 (Bethyl A301-458A). .. 10ug of antibody was incubated with Protein A/G agarose beads (Pierce) for 1hr at room temperature.

    other:

    Article Title: Molecular mechanisms for CFIm-mediated regulation of mRNA alternative polyadenylation
    Article Snippet: CPSF100 , Bethyl , A301-581A; RRID:AB_1078861.



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    Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
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    Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
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    Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
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    Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( <t>CPSF2</t> ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.
    Anti Cpsf73, supplied by Fortis Life Sciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( CPSF2 ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.

    Journal: Nucleic Acids Research

    Article Title: eIF2D promotes 40S ribosomal subunit recycling during intrinsic ribosome destabilization

    doi: 10.1093/nar/gkaf1322

    Figure Lengend Snippet: Decreased IRD-inducing protein levels and altered splicing patterns in eIF2D-deficient cells. ( A ) Cumulative fraction of the fold changes in protein levels in eIF2D KO cells relative to the control cells ( n = 4 biologically independent samples). Protein levels were analyzed via DIA-MS, and the results are shown for all detected, short nascent chain, and long nascent chain proteins. P -values were calculated using the two-tailed Mann–Whitney U test. ( B ) Differences in the median log 2 fold changes in protein levels between the indicated cell lines and control cells. ** P < .01 and *** P < .001; NS, not significant (two-tailed Mann–Whitney U test). ( C ) Gene Ontology (GO) term analysis of IRD target genes with reduced protein levels in eIF2D KO cells. FDR, false discovery rate. ( D ) Volcano plots showing the differences in the PSI scores of skipped exons between the eIF2D KO and control cells ( n = 2 biologically independent samples). Gray dashed lines indicate a ∆PSI of ±0.05 and an FDR of 0.05. ( E ) Numbers of skipped and retained introns in the eIF2D KO, eIF2A KO, and MCTS1 KO cells compared to those isplicing, and transcripn the control cells. Alternative splicing events not consistently altered in two independent clones were excluded. ( F ) Cleavage and polyadenylation specific factor 2 ( CPSF2 ) gene structure and Sashimi plots showing the differential inclusion of CPSF2 exon 14. Representative data of two replicates are shown. ( G ) Immunoblotting analysis of WT, eIF2D KO, and MCTS1 KO cells using the indicated antibodies. HSP90 was used a loading control.

    Article Snippet: Primary antibodies against MCTS1 (#GTX117793; GeneTex), DENR (203057-T46; Sino biologicals), eIF2D (12840-1-AP; Proteintech), CPSF2 (A301-581A; Bethyl Laboratories), HSP90 (610 419; BD Biosciences), and V5 epitope (R960CUS; Thermo Fisher Scientific) were used in this study.

    Techniques: Control, Two Tailed Test, MANN-WHITNEY, Alternative Splicing, Clone Assay, Western Blot